ID G1MUJ7_MELGA Unreviewed; 636 AA.
AC G1MUJ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Acetoacetyl-CoA synthetase {ECO:0000256|ARBA:ARBA00015326, ECO:0000256|RuleBase:RU367019};
DE EC=6.2.1.16 {ECO:0000256|ARBA:ARBA00012988, ECO:0000256|RuleBase:RU367019};
GN Name=AACS {ECO:0000313|Ensembl:ENSMGAP00000002214.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000002214.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000002214.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000002214.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol.
CC {ECO:0000256|RuleBase:RU367019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:16117, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; EC=6.2.1.16;
CC Evidence={ECO:0000256|RuleBase:RU367019};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU367019}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU367019}.
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DR AlphaFoldDB; G1MUJ7; -.
DR Ensembl; ENSMGAT00000002889.3; ENSMGAP00000002214.2; ENSMGAG00000002563.3.
DR GeneTree; ENSGT00940000156044; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OMA; MPNTWQT; -.
DR TreeFam; TF354241; -.
DR Proteomes; UP000001645; Chromosome 17.
DR Bgee; ENSMGAG00000002563; Expressed in brain and 17 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367019};
KW Cytoplasm {ECO:0000256|RuleBase:RU367019};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU367019};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU367019};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU367019};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367019};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645}.
FT DOMAIN 11..68
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 74..454
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 636 AA; 70650 MW; 02C44FD4734421DB CRC64;
TNSCLLLLAN YNDLYQWSVE SFADFWAEFW KYSNIVCSRL YDEVVDTSKS IADVPEWFKG
SRLNYAENLL KHKDNDKIAL YAAKEGKEEI LKVTFEELRQ AVALYAAAMR KMGVKIGDRV
VGYLPNSIHA VEAMLAAASI GAIWSSTSPD FGINGVLDRF SQIQPKLIFS VEAVVYNGKE
HNHLEKLLSV VKGLPDLKKV VVIPYVSSRE TIDISKIPNS VFLEDFLATG KGDQAPQLEF
EQLPFSHPLF IMYSSGTTGA PKCMVHSAGG TLIQHLKEHI LHGNTTSGDI IMYYTTTGWM
MWNWLVTALA TGASVVLYDG SPLVPSPNVL WDLIDRLGIT ILGTGAKWLA VLEEKNLKPC
ETHNLQTLHT ILSTGSPLKS QSYEYVYKHI KSSVLLGSIS GGTDIISCFM GQNVTIPVYK
GEIQARNLGM AVEAWNDEGK PVWGESGELV CTKPIPCQPT HFWNDENGSK YRKAYFSKFP
GVWAHGDYCK INPKTGGIVM LGRSDGTLNP NGVRFGSSEI YNIVEAFEEV SDSLCVPQYN
KDGEERVILF LKMASNHAFS EDLVKRIRDA IRVALSARHV PSLILETKGI PYTINGKKVE
VAVKQIIAGK EVEQRGAFSN PETLDLYQNI PELQNF
//
